cooperativity

co·op·er·a·tiv·i·ty

(kō-op'er-ă-tiv'i-tē),

A property of certain proteins (often enzymes) in which the binding curves or saturation curves or, in the case of enzymes, a plot of initial rates as a function of initial substrate concentration, are nonhyperbolic; suggests that the binding of a ligand has a different affinity at different ligand concentrations. Both allosterism and hysteresis display cooperativity. Compare: allosterism, hysteresis.

cooperativity

/co·op·er·a·tiv·i·ty/ (ko-op″er-ah-tiv´ĭ-te) the phenomenon of alteration in binding of subsequent ligands upon binding of an initial ligand by an enzyme, receptor, or other molecule with multiple binding sites; the affinity for further binding may be enhanced (positive c.) or decreased (negative c.) .

cooperativity

interaction between some proteins in which the binding of one may increase or decrease binding of the other.

In ligand-receptor binding kinetics, for example, the equation is strictly valid only for simultaneous binding of all ligand molecules; for the more likely sequential or independent binding schemes, it applies only for strong positive cooperativity [5,6].

Recently, cognitive narratologists have begun to extend the meaning of the notions "cognition" and mind so as to include aspects of communication and interaction ("affect, cooperativity, exteriority and contextuality" [Palmer 200]).

Although a large body of work has addressed how to extend the relational data model to incorporate cooperativity, neighbouring information, and/or orderings (2; 3; 10; 11; 13), neither of them have succeeded to fit into the representational and operational uniformity of traditional relational algebra or even to reach a certain degree of generality.

Depending on the [alpha] value, the binding of one substrate can favour ([alpha] < 1) or hinder ([alpha] > 1) the binding of the second substrate, leading to a positive or negative effect of allosteric cooperativity.

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